Breedlove Sophya, Crentsil Jasson, Dahal Eshan, Badano Aldo
Division of Imaging, Diagnostics, and Software Reliability, Office of Science and Engineering Laboratories, Center for Devices and Radiological Health, Food and Drug Administration, Silver Spring, MD USA.
Department of Materials Science and Engineering, Carnegie Mellon University, Pittsburgh, PA USA.
BMC Res Notes. 2020 Mar 4;13(1):128. doi: 10.1186/s13104-020-04969-8.
We present a method to prepare an amyloid model at scalable quantities for phantom studies to evaluate small-angle x-ray scattering systems for amyloid detection. Two amyloid models were made from a plasma protein with and without heating. Both models mimic the -sheet structure of the -amyloid () plaques in Alzheimer's disease. Amyloid detection is based on the distinct peaks in the scattering signature of the -sheet structure. We characterized the amyloid models using a spectral small-angle x-ray scattering (sSAXS) prototype with samples in a plastic syringe and within a cylindrical polymethyl methacrylate (PMMA) phantom.
sSAXS data show that we can detect the scattering peaks characteristic of amyloid -sheet structure in both models around 6 and 13 . The model prepared without heating provides a stronger signal in the PMMA phantom. The methods described can be used to prepare models in sufficiently large quantities and used in samples with different packing density to assess the performance of quantification systems.
我们提出一种方法，可制备可扩展数量的淀粉样蛋白模型用于体模研究，以评估用于淀粉样蛋白检测的小角X射线散射系统。通过对一种血浆蛋白进行加热和不加热处理制备了两种淀粉样蛋白模型。两种模型均模拟阿尔茨海默病中β-淀粉样蛋白（Aβ）斑块的β-折叠结构。淀粉样蛋白检测基于β-折叠结构散射特征中的明显峰。我们使用光谱小角X射线散射（sSAXS）原型对淀粉样蛋白模型进行了表征，样品置于塑料注射器中以及圆柱形聚甲基丙烯酸甲酯（PMMA）体模内。
sSAXS数据表明，我们能够在两种模型中检测到约6和13处淀粉样蛋白β-折叠结构的特征散射峰。未加热制备的Aβ模型在PMMA体模中提供更强的信号。所描述的方法可用于大量制备模型，并用于不同堆积密度的样品中，以评估Aβ定量系统的性能。
